Reviewed, UniProtKB/Swiss-Prot Q2M3T9 (HYAL4_HUMAN)

Names and origin

Protein names

Recommended name:
    Hyaluronidase-4
      Short name=Hyal-4
    EC=3.2.1.35
Alternative name(s):
    Hyaluronoglucosaminidase-4

Gene names

Name:

HYAL4

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	481 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at transcript level.

General annotation (Comments)

Function	Endo-hyaluronidase that degrades hyaluronan to smaller oligosaccharide fragments. Has also chondroitase activity. Ref.5
Catalytic activity	Random hydrolysis of (1->4)-linkages between N-acetyl-beta-D-glucosamine and D-glucuronate residues in hyaluronate.
Subcellular location	Membrane; Multi-pass membrane protein Potential.
Tissue specificity	Detected in placenta and skeletal muscle. Ref.1
Sequence similarities	Belongs to the glycosyl hydrolase 56 family.

Ontologies

Keywords
Cellular component	Membrane
Coding sequence diversity	Polymorphism
Domain	EGF-like domain Transmembrane
Molecular function	Glycosidase Hydrolase
PTM	Disulfide bond Glycoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	fusion of sperm to egg plasma membrane Inferred from electronic annotation. Source: InterPro glycosaminoglycan catabolic process Ref.1 Traceable author statement. Source: ProtInc
Cellular component	integral to membrane Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	hyalurononglucosaminidase activity Ref.1 Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 481	481	Hyaluronidase-4		PRO_0000301999
Regions
	Topological domain	1 – 8	8	Cytoplasmic Potential
	Transmembrane	9 – 29	21	Potential
	Topological domain	30 – 453	424	Extracellular Potential
	Transmembrane	454 – 474	21	Potential
	Topological domain	475 – 481	7	Cytoplasmic Potential
Sites
	Active site	147	1	Proton donor By similarity
Amino acid modifications
	Glycosylation	86	1	N-linked (GlcNAc...) Potential
	Glycosylation	115	1	N-linked (GlcNAc...) Potential
	Glycosylation	343	1	N-linked (GlcNAc...) Potential
	Disulfide bond	59 ↔ 351		By similarity
	Disulfide bond	223 ↔ 237		By similarity
	Disulfide bond	376 ↔ 387		By similarity
	Disulfide bond	381 ↔ 435		By similarity
	Disulfide bond	437 ↔ 446		By similarity
Natural variations
	Natural variant	346	1	A → S: dbSNP rs6949082. Ref.4		VAR_034936
Experimental info
	Sequence conflict	263	1	G → C in AAC98883. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Q2M3T9-1 [UniParc]. Last modified September 11, 2007. Version 2. Checksum: 9D530009AA898D1F	FASTA	481	54,249
	10 20 30 40 50 60 MKVLSEGQLK LCVVQPVHLT SWLLIFFILK SISCLKPARL PIYQRKPFIA AWNAPTDQCL 70 80 90 100 110 120 IKYNLRLNLK MFPVIGSPLA KARGQNVTIF YVNRLGYYPW YTSQGVPING GLPQNISLQV 130 140 150 160 170 180 HLEKADQDIN YYIPAEDFSG LAVIDWEYWR PQWARNWNSK DVYRQKSRKL ISDMGKNVSA 190 200 210 220 230 240 TDIEYLAKVT FEESAKAFMK ETIKLGIKSR PKGLWGYYLY PDCHNYNVYA PNYSGSCPED 250 260 270 280 290 300 EVLRNNELSW LWNSSAALYP SIGVWKSLGD SENILRFSKF RVHESMRIST MTSHDYALPV 310 320 330 340 350 360 FVYTRLGYRD EPLFFLSKQD LVSTIGESAA LGAAGIVIWG DMNLTASKAN CTKVKQFVSS 370 380 390 400 410 420 DLGSYIANVT RAAEVCSLHL CRNNGRCIRK MWNAPSYLHL NPASYHIEAS EDGEFTVKGK 430 440 450 460 470 480 ASDTDLAVMA DTFSCHCYQG YEGADCREIK TADGCSGVSP SPGSLMTLCL LLLASYRSIQ L

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Expression analysis of six paralogous human hyaluronidase genes clustered on chromosomes 3p21 and 7q31." Csoka A.B., Scherer S.W., Stern R. Genomics 60:356-361(1999) [PubMed: 10493834] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.
[2]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"Human chromosome 7: DNA sequence and biology." Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S. , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C. Science 300:767-772(2003) [PubMed: 12690205] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT SER-346. Tissue: Cerebellum.
[5]	"Structures of vertebrate hyaluronidases and their unique enzymatic mechanism of hydrolysis." Jedrzejas M.J., Stern R. Proteins 61:227-238(2005) [PubMed: 16104017] [Abstract] Cited for: FUNCTION, 3D-STRUCTURE MODELING.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF009010 mRNA. Translation: AAC98883.1. AC006029 Genomic DNA. Translation: AAD43186.1. CH236947 Genomic DNA. Translation: EAL24331.1. BC104788 mRNA. Translation: AAI04789.1. BC104790 mRNA. Translation: AAI04791.1.
IPI	IPI00099438.
RefSeq	NP_036401.2.
UniGene	Hs.28673
3D structure databases
ModBase	Search...
Protein family/group databases
CAZy	GH56. Glycoside Hydrolase Family 56.
Proteomic databases
PRIDE	Q2M3T9.
Genome annotation databases
Ensembl	ENSG00000106302. Homo sapiens. [Contig view]
GeneID	23553.
KEGG	hsa:23553.
UCSC	uc003vlc.1. human.
Organism-specific databases
GeneCards	GC07P123272.
HGNC	HGNC:5323. HYAL4.
MIM	604510. gene.
PharmGKB	PA29574.
GenAtlas	Search...
Phylogenomic databases
HOGENOM	Q2M3T9.
HOVERGEN	Q2M3T9.
OMA	Q2M3T9. YLAKATF.
Enzyme and pathway databases
BRENDA	3.2.1.35. 247.
Gene expression databases
ArrayExpress	Q2M3T9.
Bgee	Q2M3T9.
CleanEx	HS_HYAL4.
Family and domain databases
InterPro	IPR013785. Aldolase_TIM. IPR006210. EGF-like. IPR013032. EGF-like_reg_CS. IPR017430. Glyco_hydro_56_Hyaluronidase. IPR001439. Glyco_hydro_56_PH20. IPR001968. Glycoside_hydrolase_family_56. IPR018155. Hyaluronidase. [Graphical view]
Gene3D	G3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
PANTHER	PTHR11769. Glyco_hydro_56. 1 hit.
Pfam	PF01630. Glyco_hydro_56. 1 hit. [Graphical view]
PIRSF	PIRSF038193. Hyaluronidase. 1 hit.
PRINTS	PR00846. GLHYDRLASE56. PR00848. SPERMPH20.
ProDom	PD003549. Glyco_hydro_56. 1 hit. [Graphical view] [Entries sharing at least one domain]
SMART	SM00181. EGF. 1 hit. [Graphical view]
PROSITE	PS00022. EGF_1. 1 hit. PS01186. EGF_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	46112.
SOURCE	Search...

Entry information

Entry name

HYAL4_HUMAN

Accession

Primary (citable) accession number: Q2M3T9
Secondary accession number(s): Q9UL99, Q9Y6T9

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	September 11, 2007
Last modified:	July 7, 2009
This is version 37 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)